Linked Life Data

7744864

Source:http://linkedlifedata.com/resource/pubmed/id/7744864

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1995-6-12
pubmed:abstractText
We reported previously that recombinant myristoylated, alanine-rich protein kinase C substrate (MARCKS) expressed in Escherichia coli as well as MARCKS purified from rat brain specifically bound to phosphatidylserine (PS) in a calcium-independent manner and that the binding was regulated through phosphorylation of MARCKS (Nakaoka, T., Kojima, N., Hamamoto, T., Kurosawa, N., Lee, Y. C., Kawasaki, H., Suzuki, K., and Tsuji, S. (1993) J. Biochem. (Tokyo) 114, 449-452). In this study, to identify the minimum PS-binding region of MARCKS and the regulatory phosphorylation site, the binding of MARCKS to PS was examined in deletion mutants producing glutathione S-transferase (GST) fusion proteins. The mutant proteins GST-6-180 and GST-127-160 had almost the same ability to bind to immobilized PS as MARCKS purified from rat brain, whereas GST-127-152 did not bind to it. In addition, the binding of GST-6-156 to immobilized PS was 62% of that of GST-6-180, but that of GST-6-152 was only 8% and that of GST-6-135 was not detected. The effect of phosphorylation by protein kinase C was examined in several mutants of GST-6-180 whose serine residues were substituted with alanine. After phosphorylation, the mutants GST-6-180[S156A and S163A], GST-6-180]S156A], and GST-6-180[S163A] did not bind to immobilized PS like native MARCKS and GST-6-180. However, even after phosphorylation, GST-6-180-[S152A] and GST-6-180[S152A and S156A] could bind to immobilized PS. These results strongly suggest that MARCKS binds to PS molecules in the inner leaflet of the plasma membrane through residues 127-156, with residues 153-156 (FKKS) being particularly important in the binding of MARCKS to PS, and that the binding is regulated through the protein kinase C-catalyzed phosphorylation of the serine at residue 152.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12147-51
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7744864-Amino Acid Sequence, pubmed-meshheading:7744864-Animals, pubmed-meshheading:7744864-Base Sequence, pubmed-meshheading:7744864-Binding Sites, pubmed-meshheading:7744864-Brain Chemistry, pubmed-meshheading:7744864-Escherichia coli, pubmed-meshheading:7744864-Glutathione Transferase, pubmed-meshheading:7744864-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:7744864-Liposomes, pubmed-meshheading:7744864-Membrane Lipids, pubmed-meshheading:7744864-Membrane Proteins, pubmed-meshheading:7744864-Molecular Sequence Data, pubmed-meshheading:7744864-Mutagenesis, Site-Directed, pubmed-meshheading:7744864-Phosphatidylserines, pubmed-meshheading:7744864-Phosphorylation, pubmed-meshheading:7744864-Phosphoserine, pubmed-meshheading:7744864-Protein Binding, pubmed-meshheading:7744864-Protein Kinase C, pubmed-meshheading:7744864-Protein Processing, Post-Translational, pubmed-meshheading:7744864-Proteins, pubmed-meshheading:7744864-Rats, pubmed-meshheading:7744864-Recombinant Fusion Proteins, pubmed-meshheading:7744864-Sequence Deletion
pubmed:year
1995
pubmed:articleTitle
Characterization of the phosphatidylserine-binding region of rat MARCKS (myristoylated, alanine-rich protein kinase C substrate). Its regulation through phosphorylation of serine 152.
pubmed:affiliation
Fourth Department of Internal Medicine, School of Medicine, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't